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| Product Category: | Human Adenovirus Type5 (dE1/E3) expressing Matrix Metalloproteinase 2 (gelatinase A, 72kDa Gelatinase, 72kDa Type IV Collagenase) (MMP2) under a CMV promoter. |
| Description: | Matrix Metalloproteinase 2 (gelatinase A, 72kDa Gelatinase, 72kDa Type IV Collagenase), pre-packaged adenovirus, ready to ship and ready to use format. |
| Gene: | Matrix Metalloproteinase 2 (gelatinase A, 72kDa Gelatinase, 72kDa Type IV Collagenase) |
| NCBI Acc. #: | BC002576 |
| Gene ID: | 4313 |
| GI Number: | 12803498 |
| Fusion Tag: | No |
| Promoter: | CMV |
| Titer: | 1x1010~1x1011 PFU/ml |
| Storage Buffer: | DMEM with 2.5% BSA, 2.5% glycerol |
| Background: | MMP (matrix metalloproteinase) are proteolytic enzymes capable of degrading connective tissue components. MMP have a common mode of activation, a conserved amino acid sequence in the putative metal binding-active site region, and are inhibited by specific tissue inhibitors of metalloproteinases (TIMPs). MMPa and TIMPs play a significant role in regulating angiogenesis. MMP2 is synthesized as a 631 amino acid proenzyme which is activated by cleavage of the first 80 amino acids, and contains the basic structure of propeptide, catalytic, and hemopexin domains. The matrix metalloproteinases (MMPs) are a family of at least eighteen secreted and membrane-bound zincendopeptidases. Collectively, these enzymes can degrade all the components of the extracellular matrix, including fibrillar and non-fibrillar collagens, fibronectin, laminin and basement membrane glycoproteins. In general, a signal peptide, a propeptide, and a catalytic domain containing the highly conserved zinc-binding site characterizes the structure of the MMPs. Functionally, MMP2 is involved in tissue remodeling. Mutations in MMP-2 gene have been associated with Winchester syndrome and Nodulosis-Arthropathy-Osteolysis (NAO) syndrome. Two transcript variants encoding different isoforms of MMP-2 have been found. |
| Documents: | Please contact us to request the manual |
